Immobilized Enzyme-Based Microtiter Plate Assay for Glucose in Foods

Ukeda, Hiroyuki; Fujita, Yoshihiro; Ohira, Miki; Sawamura, Masayoshi

doi:10.1021/jf960261l

Cited by 24 publications

(26 citation statements)

References 16 publications

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“…Because the formation of polymerized glutaraldehyde during the activation reaction was important to obtain higher activity of the immobilized GOD in our previous report 2 , the reaction conditions of glutaraldehyde that affected its formation were studied: for example, the reaction pH and the reaction time. Figure 1 depicts the effect of the reaction pH of glutaraldehyde on the activity of the immobilized AOD, where the values indicate the absorbance change for 30 min.…”

Section: Immobilization Of Aodmentioning

confidence: 99%

“…1 We recently proposed a novel analytical method based on immobilized enzymes in which a 96-well microtiter plate with immobilized enzymes is used as the integrated reaction vessel. 2 The 96-well microtiter plate has been widely used for enzyme-immunometric assays (EIA) and the configuration is suitable for integrating the reaction vessel with immobilized enzymes. Glucose oxidase (GOD) and peroxidase (POD) immobilized on the surface of the microtiter plate were stable and applicable to the determination of D-glucose in practical food samples.…”

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confidence: 99%

“…Glucose oxidase (GOD) and peroxidase (POD) immobilized on the surface of the microtiter plate were stable and applicable to the determination of D-glucose in practical food samples. 2 For the purpose of developing the principle, in the present investigation, a determination system for ethanol was constructed and applied to practical alcoholic beverages. The method is based on the enzyme reaction of alcohol oxidase (AOD) and POD, and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) is used as an electron donor for POD.…”

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Immobilized Enzyme-Based Microtiter Plate Assay for Ethanol in Alcoholic Beverages

1999

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A method for the determination of ethanol using alcohol oxidase (AOD), peroxidase (POD), and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) was developed in which those enzymes were separately immobilized on the inside surface of each well of a 96-well microtiter plate. Prior to immobilization, the surface was activated with glutaraldehyde. The activation conditions remarkably affected the activity of the immobilized AOD. A sample solution containing ethanol was first added into the well with immobilized AOD (AOD-well). After 30 min, an aliquot (20 µl) was transferred into the well with immobilized POD containing 180 µl of 2 mM ABTS and the absorbance change at 415 nm for 10 min was measured with a microplate reader. The calibration curve was linear over the range 0.10 -1.0 mM, and the relative standard deviation (n=5) was 0.8% for 1 mM ethanol. The ethanol concentration in alcoholic beverages, obtained by the present method, agreed well with that by the F-kit method. The AOD-well was reusable for 20 successive determinations.

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Section: Immobilization Of Aodmentioning

confidence: 99%

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confidence: 99%

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Immobilized Enzyme-Based Microtiter Plate Assay for Ethanol in Alcoholic Beverages

1999

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“…For instance, Ukeda et al developed a spectrophotometric system which used immobilized enzymes on the surface of the micro titer plate. [17][18][19]268 U/mg-solid) and mutarotase (MUT, EC 5. …”

Section: Introductionmentioning

confidence: 99%

“…For instance, Ukeda et al developed a spectrophotometric system which used immobilized enzymes on the surface of the micro titer plate. [17][18][19] Recently, a multi-channel dissolved oxygen meter (DOX96) was developed with the intention of making simultaneous evaluations of drug resistance for microorganisms. 20 Arai et al inoculated mixtures of a test drug and a culture medium containing microorganisms in the wells of the electrode plate (96-wells, MEC-96), and evaluated the drug resistance by monitoring the oxygen consumption accompanying the respiration of viable microorganisms.…”

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A Novel Method for the Assay of α-Glucosidase Inhibitory Activity Using a Multi-channel Oxygen Sensor

et al. 2002

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Noninsulin-dependent diabetes mellitus (NIDDM), which is a major adult disease, is caused by a secretary decrease of insulin from pancreatic Langerhans β cells, or a lowering of the insulin resistance. 1 One of the most direct and beneficial types of therapy for NIDDM is achieved by control of the blood glucose level after a meal by delaying glucose absorption. 2 Among the therapeutic drugs used to prevent a high blood glucose level, the inhibitors of α-glucosidase (AGH, EC 3.2.1.20), which is a membrane-bound enzyme at the epithelium of the small intestine that catalyzes the cleavage of glucose from disaccharide, are effective for delaying glucose absorption. 3,4 To date, certain synthetic inhibitors of AGH 5 have been developed and used for the therapeutic treatment of NIDDM. 6 In the field of food chemistry, much attention has been devoted to a search for food materials with AGH inhibitory activity from natural resources and that have a high demand for a rapid and continuous assay method of AGH inhibitory activity. A spectrophotometric method using a pseudo-substrate, pnitrophenyl-α-D-glucopyranoside, and free AGH from baker's yeast has been widely used for in vitro assays. 7,8 It was pointed out, however, that the evaluated inhibitory effects of pharmaceuticals did not match with those obtained by an in vivo experiment. 9 The reason for this discordance comes from the difference in the environment of AGH in the mammalian intestine. We previously reported on a pseudo-in vivo assay system using immobilized rat intestinal AGH on Sepharose, which mimics the environment of the mammalian small intestine. 10 Biosensors still offer great potential as the next revolution in analysis. The high sensitivity of enzymes coupled with the electrochemical signal transducer should ideally result in an enzyme electrode capable of measuring the concentration of the substrate in a medium containing a diverse mixture of other compounds. 11 So far, the development of biosensors has focused on the system for a single channel. The development of a system for multi-channel biosensors is very important to increase the frequency of the sample treatment. We have been devoted to the development of multi-channel flow-type biosensors. 12-16 A micro titer plate detection system with 96-wells is another type of multi-channel detection system using immobilized enzymes. For instance, Ukeda et al. developed a spectrophotometric system which used immobilized enzymes on the surface of the micro titer plate. [17][18][19] Recently, a multi-channel dissolved oxygen meter (DOX96) was developed with the intention of making simultaneous evaluations of drug resistance for microorganisms. 20 Arai et al. inoculated mixtures of a test drug and a culture medium containing microorganisms in the wells of the electrode plate (96-wells, MEC-96), and evaluated the drug resistance by monitoring the oxygen consumption accompanying the respiration of viable microorganisms. 21 These kinds of evaluations, however, were qualitative with respect to measurements of th...

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Interaction of Ionic Liquids with Polysaccharides, 8 – Synthesis of Cellulose Sulfates Suitable for Polyelectrolyte Complex Formation

Gericke

Liebert

Heinze

2009

Macromolecular Bioscience

112

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Water-soluble CS with different DS were synthesized by homogeneous conversion of cellulose (microcrystalline cellulose and spruce sulfite pulp) with different sulfating agents in the ionic liquids BMIMCl, AMIMCl and EMIMAc. N,N-Dimethylformamide was used as a dipolar aprotic co-solvent in order to improve the miscibility of the reaction mixture. The CS prepared by the new homogeneous reaction pathway were studied towards the formation of PEC capsules. CS obtained from SSP formed mechanically stable PEC capsules with PolyDADMAC. Exploiting this method, the microencapsulation of glucose oxidase was studied and enzyme activity tests were performed with encapsulated GOD.

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Immobilized Enzyme-Based Microtiter Plate Assay for Glucose in Foods

Cited by 24 publications

References 16 publications

Immobilized Enzyme-Based Microtiter Plate Assay for Ethanol in Alcoholic Beverages

Immobilized Enzyme-Based Microtiter Plate Assay for Ethanol in Alcoholic Beverages

A Novel Method for the Assay of α-Glucosidase Inhibitory Activity Using a Multi-channel Oxygen Sensor

Interaction of Ionic Liquids with Polysaccharides, 8 – Synthesis of Cellulose Sulfates Suitable for Polyelectrolyte Complex Formation

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